These compounds each functioned as irreversible inactivators of the ASADH isolated from Candida albicans (C. albicans), a pathogenic fungal species. Changes in the identity of R2 result in higher affinity, increased inactivation rates, and improvements in the ratio of inactivation rate (kinact) to affinity (Ki) that serves as a measure of covalent inactivator efficiency (Table 1, top). Further increases in target affinity are observed with changes to R1 (Table 1, bottom). ASADH: aspartate β-semialdehyde dehydrogenase.
Declarations
Acknowledgments
The author thanks Samantha Friday (Ohio University) for conducting the kinetic studies on ASADH, and Dr. Chris Halkides (University of North Carolina Wilmington) for providing the vinyl sulfones used in the ASADH inactivation studies.
Author contributions
REV: Conceptualization, Writing—original draft, Writing—review & editing. The author read and approved the submitted version.
Conflicts of interest
The author declares that there are no conflicts of interest.
Open Exploration maintains a neutral stance on jurisdictional claims in published institutional affiliations and maps. All opinions expressed in this article are the personal views of the author(s) and do not represent the stance of the editorial team or the publisher.
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